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PDBsum entry 4nle

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protein Protein-protein interface(s) links
Lyase PDB id
4nle
Jmol
Contents
Protein chains
464 a.a.
Waters ×502
PDB id:
4nle
Name: Lyase
Title: Crystal structure of apo adenylosuccinate lyase from mycobac smegmatis
Structure: Adenylosuccinate lyase. Chain: a, b. Engineered: yes
Source: Mycobacterium smegmatis. Organism_taxid: 246196. Strain: mc2 155. Gene: msmeg_5847, purb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.16Å     R-factor:   0.206     R-free:   0.238
Authors: S.Banerjee,M.R.N.Murthy
Key ref: S.Banerjee et al. (2014). Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme. FEBS J, 281, 1642-1658. PubMed id: 24479855 DOI: 10.1111/febs.12730
Date:
14-Nov-13     Release date:   05-Mar-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0R4I6  (A0R4I6_MYCS2) -  Adenylosuccinate lyase
Seq:
Struc:
474 a.a.
464 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.4.3.2.2  - Adenylosuccinate lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Purine Biosynthesis (late stages)
      Reaction:
1. N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
2. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide
N(6)-(1,2-dicarboxyethyl)AMP
= fumarate
+ AMP
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate
= fumarate
+ 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     'de novo' AMP biosynthetic process   4 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1111/febs.12730 FEBS J 281:1642-1658 (2014)
PubMed id: 24479855  
 
 
Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme.
S.Banerjee, M.J.Agrawal, D.Mishra, S.Sharan, H.Balaram, H.S.Savithri, M.R.Murthy.
 
  ABSTRACT  
 
No abstract given.